5L2X

Crystal structure of human PrimPol ternary complex

5L2X の概要

• エントリーDOI: 10.2210/pdb5l2x/pdb
• 分子名称: DNA-directed primase/polymerase protein, DNA (5'-D(P*TP*CP*GP*CP*(5IU)P*AP*CP*C)-3'), DNA (5'-D(P*GP*GP*TP*AP*GP*CP*(DDG))-3'), ... (6 entities in total)
• 機能のキーワード: protein-dna complex, transferase-dna complex, transferase/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: Q96LW4
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 101354.75

構造登録者

Rechkoblit, O.,Gupta, Y.K.,Malik, R.,Rajashankar, K.R.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K. (登録日: 2016-08-02, 公開日: 2016-11-23, 最終更新日: 2024-03-06)

主引用文献

Rechkoblit, O.,Gupta, Y.K.,Malik, R.,Rajashankar, K.R.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K.
Structure and mechanism of human PrimPol, a DNA polymerase with primase activity.
Sci Adv, 2:e1601317-e1601317, 2016

PubMed Abstract: PrimPol is a novel human enzyme that contains both DNA primase and DNA polymerase activities. We present the first structure of human PrimPol in ternary complex with a DNA template-primer and an incoming deoxynucleoside triphosphate (dNTP). The ability of PrimPol to function as a DNA primase stems from a simple but remarkable feature-almost complete lack of contacts to the DNA primer strand. This, in turn, allows two dNTPs to bind initiation and elongation sites on the enzyme for the formation of the first dinucleotide. PrimPol shows the ability to synthesize DNA opposite ultraviolet (UV) lesions; however, unexpectedly, the active-site cleft of the enzyme is constrained, which precludes the bypass of UV-induced DNA lesions by conventional translesion synthesis. Together, the structure addresses long-standing questions about how DNA primases actually initiate synthesis and how primase and polymerase activities combine in a single enzyme to carry out DNA synthesis.

PubMed: 27819052
DOI: 10.1126/sciadv.1601317

実験手法

X-RAY DIFFRACTION (2.2 Å)